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==NMR solution structure of the N terminal domain of subunit E (E1-52) of A1AO ATP synthase from Methanocaldococcus jannaschii== | ==NMR solution structure of the N terminal domain of subunit E (E1-52) of A1AO ATP synthase from Methanocaldococcus jannaschii== | ||
<StructureSection load='2kk7' size='340' side='right'caption='[[2kk7 | <StructureSection load='2kk7' size='340' side='right'caption='[[2kk7]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2kk7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2kk7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KK7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KK7 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2kk7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kk7 OCA], [https://pdbe.org/2kk7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kk7 RCSB], [https://www.ebi.ac.uk/pdbsum/2kk7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kk7 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2kk7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kk7 OCA], [https://pdbe.org/2kk7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kk7 RCSB], [https://www.ebi.ac.uk/pdbsum/2kk7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kk7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/VATE_METJA VATE_METJA] Produces ATP from ADP in the presence of a proton gradient across the membrane (By similarity). | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Methanocaldococcus jannaschii]] | [[Category: Methanocaldococcus jannaschii]] | ||
[[Category: | [[Category: Balakrishna A]] | ||
[[Category: | [[Category: Gayen S]] | ||
[[Category: Gruber G]] | |||
Latest revision as of 15:51, 20 December 2023
NMR solution structure of the N terminal domain of subunit E (E1-52) of A1AO ATP synthase from Methanocaldococcus jannaschiiNMR solution structure of the N terminal domain of subunit E (E1-52) of A1AO ATP synthase from Methanocaldococcus jannaschii
Structural highlights
FunctionVATE_METJA Produces ATP from ADP in the presence of a proton gradient across the membrane (By similarity). Publication Abstract from PubMedThe N-termini of E and H of A1AO ATP synthase have been shown to interact and an NMR structure of N-terminal H1-47 has been solved recently. In order to understand the E-H assembly and the N-terminal structure of E, the truncated construct E1-52 of Methanocaldococcus jannaschii A1AO ATP synthase was produced, purified and the solution structure of E1-52 was determined by NMR spectroscopy. The protein is 60.5 A in length and forms an alpha helix between the residues 8-48. The molecule is amphipathic with a strip of hydrophobic residues, discussed as a possible helix-helix interaction with neighboring subunit H. NMR solution structure of the N-terminal domain of subunit E (E1-52) of A1AO ATP synthase from Methanocaldococcus jannaschii.,Gayen S, Balakrishna AM, Gruber G J Bioenerg Biomembr. 2009 Aug;41(4):343-8. PMID:19760172[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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